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Reviewed, UniProtKB/Swiss-Prot A0A390 (NU1C_COFAR)

Last modified June 16, 2009. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
    EC=1.6.5.-
Alternative name(s):
    NAD(P)H dehydrogenase subunit 1
      Short name=NDH subunit 1
    NADH-plastoquinone oxidoreductase subunit 1
Gene names
Name: ndhA
Encoded onPlastid; Chloroplast
OrganismCoffea arabica (Coffee)
Taxonomic identifier13443 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsGentianalesRubiaceaeIxoroideaeCoffeeaeCoffea

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient By similarity.

Catalytic activity

NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01350

Subunit structure

NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus By similarity.

Subcellular location

Plastidchloroplast thylakoid membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the complex I subunit 1 family.

Ontologies

Keywords
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   DomainTransmembrane
   LigandNAD
NADP
Plastoquinone
   Molecular functionOxidoreductase
   PTMQuinone
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: HAMAP

   Cellular componentchloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic HAMAP MF_01350
PRO_0000275578

Regions

Transmembrane26 – 4621 Potential
Transmembrane98 – 11821 Potential
Transmembrane127 – 14721 Potential
Transmembrane246 – 26621 Potential
Transmembrane268 – 28821 Potential
Transmembrane300 – 32021 Potential
Transmembrane336 – 35621 Potential

Sequences

Sequence LengthMass (Da)Tools
A0A390-1 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: AE7A8C8B0E83BD1C

FASTA36340,160
        10         20         30         40         50         60 
MIIDTTELQA INSFFKLESL KEVYGIIWIL IPIFTLVLGI TIGVLVIVWL EREISAGIQQ 

        70         80         90        100        110        120 
RIGPEYAGPL GILQALADGT KLLFKENLLP SRGDARLFSI GPSIAVISIL LSYSVIPFGY 

       130        140        150        160        170        180 
RLVLADLTIG VFLWIAISSI APIGLLMSGY GSNNKYSFLG GLRAAAQSIS YEIPLTLCVL 

       190        200        210        220        230        240 
SISLLSNSSS TVDIVEAQSK YGFWGWNLWR QPIGFIIFLI SSLAECERLP FDLPEAEEEL 

       250        260        270        280        290        300 
VAGYQTEYSG IKFGLFYVAS YLNLLVSSLF VTVLYLGGWN LSIPYIFVSE IFDINKAGKV 

       310        320        330        340        350        360 
FGPVIGIFIT LAKTYLFLFI PIATRWTLPR LRMDQLLNLG WKFLLPISLG NLLLTTSSQL 


LSL 

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References

[1]"The complete nucleotide sequence of the coffee (Coffea arabica L.) chloroplast genome: organization and implications for biotechnology and phylogenetic relationships amongst angiosperms."
Samson N., Bausher M.G., Lee S.-B., Jansen R.K., Daniell H.
Plant Biotechnol. J. 5:339-353(2007) [PubMed: 17309688] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EF044213 Genomic DNA. Translation: ABJ89734.1.
RefSeqYP_817537.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4421856.

Family and domain databases

HAMAPMF_01350.
[Tree]
InterProIPR001694. NADH_UbQ_OxRdtase_su1.
IPR018086. NADH_UbQ_OxRdtase_su1_CS.
[Graphical view]
PANTHERPTHR11432. Resp_NADH_DH_1. 1 hit.
PfamPF00146. NADHdh. 1 hit.
[Graphical view]
PROSITEPS00667. COMPLEX1_ND1_1. 1 hit.
PS00668. COMPLEX1_ND1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNU1C_COFAR
AccessionPrimary (citable) accession number: A0A390
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: November 14, 2006
Last modified: June 16, 2009
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents